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FAD-binding protein
This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase. [1]. 8061609. Structure of glutathione reductase from Escherichia coli at 1.86. A resolution: comparison with the enzyme from human. erythrocytes.. Mittl PR, Schulz GE. Protein Sci 1994;3:799-809. (from Pfam)
adenylyl-sulfate reductase subunit alpha
During dissimilatory sulfate reduction or sulfur oxidation, adenylylsulfate (APS) reductase catalyzes reversibly the two-electron reduction of APS to sulfite and AMP [1]. Found in several bacterial lineages and in Archaeoglobales, APS reductase is a heterodimer composed of an alpha subunit containing a noncovalently bound FAD, and a beta subunit containing two [4Fe-4S] clusters [1]. Described by this model is the alpha subunit of APS reductase, sharing common evolutionary origin with fumarate reductase/succinate dehydrogenase flavoproteins.
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